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Fear of mad cow disease, a lethal illness transmitted from infected beef to humans, has spread from Europe to the United States and around the world. Originally published to much acclaim in France, this scientific thriller, available in English for the first time and updated with a new chapter on developments in 2001, tells of the hunt for the cause of an enigmatic class of fatal brain infections, of which mad cow disease is the latest incarnation. In gripping, nontechnical prose, Maxime Schwartz details the deadly manifestations of these diseases throughout history, describes the major players and events that led to discoveries about their true nature, and outlines our current state of knowledge. The book concludes by addressing the question we all want answered: should we be afraid?
The story begins in the eighteenth century with the identification of a mysterious illness called scrapie that was killing British sheep. It was not until the 1960s that scientists understood that several animal and human diseases, including scrapie, were identical, and together identified them as transmissible spongiform encephalopathy (TSE). The various guises assumed throughout history by TSE include an illness called kuru in a cannibalistic tribe in Papua New Guinea, an infectious disease that killed a group of children who had been treated for growth hormone deficiencies, and mad cow disease. Revealing the fascinating process of scientific discovery that led to our knowledge of TSE, Schwartz relates pivotal events in the history of biology, including the Pasteurian revolution, the birth of genetics, the emergence of molecular biology, and the latest developments in biotechnology. He also explains the Nobel Prize–winning prion hypothesis, which has rewritten the rules of biological heredity and is a key link between the distinctive diseases of TSE.
Up-to-date, informative, and thoroughly captivating, How the Cows Turned Mad tells the story of a disease that continues to elude on many levels. Yet science has come far in understanding its origins, incubation, and transmission. This authoritative book is a stunning case history that illuminates the remarkable progression of science.
- Sales Rank: #1970098 in Books
- Published on: 2004-09-13
- Original language: English
- Number of items: 1
- Dimensions: 9.00" h x .63" w x 6.00" l, .82 pounds
- Binding: Paperback
- 256 pages
From The New England Journal of Medicine
In How the Cows Turned Mad, Maxime Schwartz recounts the history of the prion diseases, or subacute spongiform encephalopathies, as if writing a mystery. Schwartz refers to all the prion diseases under one rubric, "The Disease," as if a single criminal with many disguises were active. This story has truly been an exceptional one, with events that have dramatically and unexpectedly affected the economy, public health, and the political scene. We now know that there are a number of subacute spongiform encephalopathies of animals (e.g., scrapie and "mad cow disease," or bovine spongiform encephalopathy) and of humans (e.g., kuru and Creutzfeldt-Jakob disease) that are transmissible and that have similar pathologic features. The transmissible agent, a prion, is a misfolded protein (called PrP(sup Sc)) that has assumed a conformation different from that of the normal cellular form of the protein (called PrP(sup C)). In the presence of PrP(sup Sc), PrP(sup C) is converted into additional molecules of PrP(sup Sc), which then accumulates, resulting in the induction of disease. The prion is remarkable because it apparently contains no nucleic acid, triggers no immune response, causes a disease with an extraordinarily long incubation period, and is highly resistant to inactivation by physical and chemical agents (such as heat and formalin) that normally are expected to inactivate a pathogen. One of the attractive features of this book is its historical perspective, beginning with coverage of early records related to scrapie in 17th-century England and ending with a discussion of recent concerns in France about the spread of bovine spongiform encephalopathy and a new variant of Creutzfeldt-Jakob disease that has been strongly linked to bovine spongiform encephalopathy. The work of Pasteur is highlighted, presumably in part because Schwartz previously served as head of the Pasteur Institute. Schwartz reviews the many ways in which the prion diseases have surprised us and also covers recurrent themes that have frequently been overlooked. For example, in the 1930s scrapie was transmitted to sheep by means of inoculation with a formalin-treated vaccine against the virus that causes louping ill. The vaccine transmitted scrapie because it had been prepared from sheep that were presumed to have unrecognized scrapie and because scrapie resists formalin inactivation. This event presaged instances of iatrogenic spread of the subacute spongiform encephalopathies, such as one in which Creutzfeldt-Jakob disease was transmitted by the implantation of electrodes that had previously been used in an affected person and on which prions had been incompletely inactivated by formaldehyde vapor. The transmission of kuru after ritual cannibalistic ingestion of the tissues of relatives who had died of kuru reminds one of how bovine spongiform encephalopathy became endemic in cattle as a result of the ingestion of feed that contained contaminated cattle carcasses. Schwartz informs us that these events are reminiscent of a still earlier event recognized by Nocard, a student of Pasteur, in which anthrax was spread from fertilizer that had been prepared from carcasses of anthrax-infected animals. The subacute spongiform encephalopathies still have much to teach us, both about their pathogenesis as well as about the role of misfolded proteins in other neurodegenerative diseases. We will need to attend to the history of these diseases carefully and also be guided by current data in order to ensure that we respond appropriately in the future to the surprises of these diseases. How the Cows Turned Mad should be understandable to readers with a relatively limited scientific background; however, it would have been helpful for Schwartz to have provided some figures to show, for example, the conversion of PrP(sup C) into PrP(sup Sc). The information about these diseases is reasonably current, with only rare errors. In the interest of space, Schwartz unfortunately was selective in his discussions of prion disease and in listing references and crediting scientists who contributed to knowledge in this field. Pasteur wrote, as cited by Schwartz, "Might it not be permitted to believe . . . that the day will come when easily utilized preventive measures will end these scourges which abruptly afflict and terrify people . . . ?" In these times of outbreaks of West Nile virus infection and the severe acute respiratory syndrome, one cannot help but think of the more cautious and somber comment of Claudius in Shakespeare's Hamlet: "Diseases desperate grown / By desperate appliance are relieved, / Or not at all." Some stories that involve intrigue and human tragedy, such as Hamlet, will always challenge us and leave unanswered questions. Raymond P. Roos, M.D.
Copyright © 2003 Massachusetts Medical Society. All rights reserved. The New England Journal of Medicine is a registered trademark of the MMS.
From Booklist
*Starred Review* Two and a half centuries ago, sheep in England started trying to scrape their wool off; in France, to shake uncontrollably. The Brits dubbed their phenomenon scrapie; the French called theirs tremblant. Between then and now, similar conditions in cows and humans were discovered and assigned the group name transmissible spongiform encephalopathies (TSEs): diseases that fill the brain with holes as in a sponge and spread from one organism to another. Their cause eluded researchers until quite recently. SOP since Pasteur sought an invasive bacterium or virus with increasingly powerful tools, which TSE agents eluded. Eventually, evidence pointed to a genetic cause involving transformation of a normal into a deviant gene by another deviant gene introduced orally into the affected organism. You had to eat something from a sick organism to become sick, and once that became popular knowledge after the concurrence of human and bovine TSE cases in England in the 1990s, there was a panic. That reaction seems unjustified; according to Schwartz, TSEs will continue to be a very minor cause of human death. Meanwhile, there may be much to learn from TSE research about such symptomatically similar illnesses as Alzheimer's disease. Writing with immense concentration and clarity, French molecular biologist Schwartz makes the long hunt for the unexpected culprit gene utterly engrossing. Ray Olson
Copyright © American Library Association. All rights reserved
Review
"An excellent overview. . . In an easily understandable way [Schwartz] explains scientific findings."--"British Medical Journal"
Most helpful customer reviews
3 of 5 people found the following review helpful.
The molecular biology is astounding
By Bruce P. Barten
This is a very complicated matter, with highly specific vocabulary that attempts to describe a variety of forms of a disease which is capable of being distinguished by different incubation periods in the various inbred species of genetically pure or altered mice that have been inoculated with transmissible spongiform encephalopathies (TSEs) in the strains that have been isolated before the French edition of this book went to press near the end of the year 2000. A key word is prion, a protein that might form part of the membrane of a normal cell. Originally in this book, prion was defined by Stanley Prusiner, winner of the Nobel Prize in 1997, in 1982 as the carrier of the infection for TSEs. "Prions are small proteinaceous infectious particles which are resistant to inactivation by most procedures that modify nucleic acids." (p. 100). Forming rods in a polymer structure, ultimately doctors, "when examining brain tissue from kuru patients, had been able to recognize what they called amyloid plaques" (pp. 101-102).
Assuming that any cow in England which showed signs of bovine spongiform encephalopathy was an indication that the entire herd had been fed contaminated meat and bone meal, (from "forty-six British plants that until 1988 had converted a total of 1.3 million metric tons of meat and bones into animal feed" p. 147), "the total number of cattle affected by the disease from the beginning of the epidemic until the end of 2000 was nearly two hundred thousand in Great Britain," (p. 151). Since the cow form of the disease and the sheep form act differently in mice who are infected, a grand experimental test was performed to see if any sheep have picked up the BSE form:
"In the summer of 2001, rumors began to circulate to the effect that the BSE agent had been found in sheep; the official outcome was to be announced at the end of the year. Europe's health authorities were in a state of red alert. If the results were positive, drastic steps would have to be taken in the sheep-farming sector. Then, just two days before the outcome was made public, there was a dramatic announcement: The researchers had made a mistake. They had mingled samples of sheep brains with samples of cattle brains--and thus there are still no data on the possible transmission of BSE to sheep in natural conditions." (p. 188).
I have noticed that when people try to assign unique numbers to anything, there is always someone who fails to notice that two of those numbers are not the same. I have even worked with a computer that had so few consecutive numbers in a field that it was not able to tell the difference between numbers that had more than the number of digits in the field. There are forty million sheep in Britain, few of which look like cows, even in that night in which all cows are black, but worse than that: the brain samples might look a lot like brain samples from a cow. This experiment was more than double blind if no one kept tract of how samples were mingled.
I love the word epizootic: "Why was an epizootic--an animal epidemic--declared at one particular time, the early 1980s, and only in the United Kingdom?" (p. 189). It must be related to "the death of six white tigers from the Bristol zoo between 1970 and 1977; they died of what was then diagnosed as a transmissible spongiform encephalopathy, but no one knows what became of the corpses. . . . After all, it isn't often that a cow eats tiger in the way that we eat beef." (p. 190). There are so many things no one knows.
3 of 3 people found the following review helpful.
Well Written, Scary as heck
By P. S. Matz
An amazing tour of the history of prion diseases. From start to finish, it's well written, beuatifully explained and frighrening. If this book hasn't scared you, read it again
2 of 2 people found the following review helpful.
Page Turner
By Rodger Shepherd
I refer the reader to the other reviews for a description of the content of the book. I simply want to align myself with those reviewers who were enthusiastic about this book. The story of the transmissable subacute spongioform encephalopies is very engagingly and authoritatively told by the author (who is a "he" - not a "she"). If you like the sort of stories that Berton Roueche wrote, then you will enjoy this book. Among other things, this book is a wonderful reminder that medicine is a constant "work in progress" and that seemingly esoteric research can suddenly become very relevant.
I would note that the book takes the story to 2003. Subsequent developments are easily tracked down with Google. I found current introductary articles on protein folding very helpful.
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